Lipases (EC 3.1.1.3) hydrolyze ester bonds of triacylglycerols and catalyze esterification and transesterification (acidolysis, alcoholysis, and interesterification) in a non-aqueous system. Some lipases, such as phospholipases, hydrolyze ester bonds in phospholipids which are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids. A 26 amino acid C-terminal peptide of Fusarium heterosporum phospholipase was described by Nagao et al., 1998, J. Biochem. 124:1124-29 to play an important role in increasing the thermostability of the lipase without the peptide having an effect on the enzymatic activity.
In light of the broad use of lipids such as e.g. as digestives, for the production of flavours, in dough and baked products of dough, as diagnostic reagents, ingredients of detergent, as catalysts of optical resolutions, etc. it would be desirable to have a mean of controlling the enzymatic activity of lipases. Furthermore, control of the lipolytic activity is desirable from a production point of view due to the option of making enzyme productions that are reproducible regarding their enzymatic activity.